Changes in the State of Hemoglobin in Patients with Coronary Heart Disease and Patients with Circulatory Failure

Abstract

Morphology of erythrocytes and conformation of hemoglobin-derived hematoporphyrin were studied in patients with coronary heart disease (CHD) and patients with circulatory failure using laser interference microscopy and Raman spectroscopy. Correlation was revealed (r=0.81) between hemoglobin oxygen saturation and oxyhemoglobin fraction in erythrocytes evaluated by Raman spectroscopy. Patients with CHD and patients with circulatory failure showed reduced oxygen-releasing capacity of hemoglobin and hemoglobin content and increased oxygen-binding capacity of hemoglobin, and hemoglobin affinity for oxygen. Significant differences from the control were observed only in patients with circulatory failure. It was found that hemoglobin content, hematocrit, and the shape of erythrocytes during CHD and circulatory failure did not differ from the control, whereas the area of erythrocytes was increased.

Role of Purinergic Receptors of Erythrocytes in the Regulation of Conformation and Oxygen- and NO-Transporting Capacity of Hemoglobin

“…The observed signifi cant increase in O 2 -binding capacity after ATP addition to erythrocyte suspension in a buffer solution means that iron atom is less submerged in the plane of the porphyrin ring; similar results were obtained for hemoglobin ability of erythrocytes in a buffer solution to donate O 2 [2,4]. Thus, ATP addition leads to increased distance between iron atom and the porphyrin ring plane.…”

“…Changes in the ratio of intensities (I) of specifi ed Raman spectrum bands refl ect changes in hematoporphyrin conformation [4], which can be interpreted as the contribution of oxyhemoglobin complexes to the total amount of hemoglobin complexes (I 1375 /(I 1375 +I 1355 ), O 2 -binding capacity of hemoglobin (I 1355 /I 1552 ), O 2 -releasing capacity of hemoglobin (I 1375 /I 1580 ), and the proportion of NO-hemoglobin complexes (I 1618 /(I 1355 +I 1375 ) [1,2,4].…”

Effect of hypoxia on the composition and state of lipids and oxygen-transport properties of erythrocyte haemoglobin

“…The characteristics of the RS spectra of Hb haemoporphyrin [24,32] are instrumental in determining the degree of oxidation of the iron atom, its spin state and the availability of ligands; and reflect changes in the structure of globin that lead to deformation of the hemoprotein and effect the oxygen-binding properties of Hb [5]. The use of RS-peaks and not their absolute values is explained by the fact that the absolute value of the spectrum intensity depends on the amount of Hb and, therefore, on the number of erythrocytes in the sample in the area of the laser focus.…”

“…Different pathologies cause changes in the amount, distribution and conformation of Hb [4][5][6][7]. Many pathological states are accompanied by development of hypoxia.…”

The effect of experimental hyperoxia on erythrocytes’ oxygen-transport function

“…They reflect the changes in the structure of globin leading to the deformation of haemoporphyrin and affecting the oxygen-binding properties of haemoglobin [52]. The conformation of haemoglobin haematoporphyrin of erythrocytes estimated in correlations of Raman spectra among healthy donors is presented in Figure 7.…”